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The Latest in Biopharm Discovery, Development, and Bioprocessing

Pall ForteBio systems have become indispensable tools at biopharmaceutical companies worldwide, resulting in a steady stream of scientific publications and presentations. This online resource will help you stay current on the latest studies featuring data from the Octet^® and BLItz^® systems. Fresh publications and presentations are captured as they become available, and can be browsed by application area or pinpointed by keyword search.

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H5N1 Vaccine-Elicited Memory B Cells Are Genetically Constrained by the IGHV Locus in the Recognition of a Neutralizing Epitope in the Hemagglutinin Stem
Wheatley A, et al., J Immunol, 195(2):602-10, 2015
Although it is becoming evident by the recent research that viral hemagglutinin (HA) could be the target for broadly neutralizing antibody responses, the frequency and phenotype of HA stem-specific B cells in vivo are yet to be revealed. This article focuses on HA stem-specific B cell responses following H5N1 vaccination and explains the re-expansion of memory B cells specific for stem epitopes. The kinetic characterization of binding between mAbs and HA were investigated using a Pall ForteBio Octet HTX system equipped with Streptavidin Biosensor probes. Biotinylated HA-trimers captured on to Streptavidin probes were used to screen against Fab of mAbs.
PubMed
Heat Shock Protein 90 Mediates the Apoptosis and Autophage in Nicotinic-Mycoepoxydiene-Treated HeLa Cells
Sun Y, et al., Acta Biochim Biophys Sin (Shanghai), 47(6):451-8, 2015
This article characterizes the interaction between Heat shock protein 90 (Hsp90) and its inhibitor nicotinicmycoepoxydiene (NMD). A Pall ForteBio Octet RED system equipped with Super-Streptavidin (SSA) biosensors was used to capture biotinylated Hsp90 binding to NMD. The KD value obtained from the Octet RED system is comparable to that obtained from a Fluorescent assay. Overall results suggest a novel mechanism pertaining to Hsp90 inhibition by NMD.
PubMed
Helicobacter Pylori FlhA Binds the Sensor Kinase and Flagellar Gene Regulatory Protein FlgS with High Affinity
Tsang J, et al., J Bacteriol, 197(11):1886-92, 2015
This study provides additional insights into flagellar assembly in Helicobacter pylori. The high affinity interaction between Flagellar Gene Regulatory Protein (Flgs) and FlhA suggest an additional role for FlhA in flagellar assembly. A Pall ForteBio Octet QK system equipped with Streptavidin Biosensor probes was used to capture biotinylated peptides representing residues 1 to 25 of FlhA. The analytes used in this investigation had FlgS or a shorter version called FlgSc.
PubMed

Featured Articles

High-Throughput Kinetic Screening of Hybridomas to Identify High-Affinity Antibodies Using Bio-Layer Interferometry
Lad L, et al., J Biomol Screen, 20(4):498-507, 2015
In this study authors have compared a traditional solid-phase enzyme-linked immunosorbent assay (ELISA) against Bio-Layer Interferometry (BLI) to screen high-affinity antibodies from hybridoma clones. A Pall ForteBio Octet RED384 instrument was used as their kinetic screening platform. This instrument was equipped with anti-mouse immunoglobulin G (IgG) Fc (AMC)-coated biosensor tips which was used to capture atibodies from hybridoma supernatants. This article also discusses about the advantages and limitations of different methods and platforms available for screening antobodies such as the flow cytometry, ELISA, electrochemiluminescence using Meso Scale Discovery (MSD) platform, and homogeneous time-resolved fluorescence (HTRF). Overall results suggest that the kinetic screening is an efficient method for identifying high-affinity antibodies.
PubMed
Identification and Structure Solution of Fragment Hits Against Kinetoplastid N-Myristoyltransferase
Robinson D, Wyatt P, Acta Crystallogr F Struct Biol Commun , 71(Pt 5):586-93, 2015
The article describes identification of new chemical hits that could occupy DDD85646 binding site of Trypanosoma brucei N-myristoyltransferase (TbNMT). This is a therapeutic target for the treatment of human African trypanosomiasis. Fragment screening was performed by ligand-observed NMR spectroscopy. Crystal structures of the identified hits were reported in complex with closely related NMT from Leishmania major. A Pall ForteBio Octet RED384 instrument equipped with Super-Streptavidin (SSA) Biosensor probes was used to obtain the binding measurements. Biotinylated TbNMT and Leishmania major N-myristoyltransferase (LmNMT) were captured onto the SSA biosensor tip surface. The fragment hits obtained from this study are smaller and possess limited complexity. Results suggest both binding-site configurations could be induced upon ligand binding, hence demonstrating conformational plasticity of the peptide-binding site.
PubMed
Improving Target Cell Specificity Using a Novel Monovalent Bispecific IgG Design
Mazor Y, et al., MAbs , 7(2):377-89, 2015
This article introduces a novel platform called DuetMab for efficient production of monovalent bispecific IgGs. It uses knobs-into-holes (KIH) methodology to heterodimerize two distinct heavy chains while increasing the efficiency of heavy and light chain pairing with an engineered disulfide bond. A Pall ForteBio Octet RED384 instrument was used in the Quantitation and Kinetic Characterization of antibodies. The concentration of DuetMab antibodies in cell-culture supernatants were measured by Protein A biosensor probes in the Quantitation mode. Whereas, the kinetic measurements of DuetMab binding to EGFR and HER2 were performed using the Octet RED384 equipped with anti-human IgG Fc capture (AHC) biosensor probes. Concurrent binding of antibodies to EGFR and HER2 were also tested on the Octet RED384 equipped with AHC and SA biosensor probes.
PubMed
In Silico Discovery and Validation of Potent Small-Molecule Inhibitors Targeting the Activation Function 2 Site of Human Oestrogen Receptor α
Singh K, et al., Breast Cancer Res, 17:27, 2015
Described herein is the identification of more potent and selective small-molecule inhibitors for a coactivator-binding pocket on oestrogen receptor-alpha (Erα). Commonly known as the activation function 2 (AF2), the interaction between AF2-binders, and the ERα protein were analyzed by Bio-Layer Interferometry (BLI) using a Pall ForteBio Octet RED instrument equipped with Super Streptavidin biosensors. Fifteen inhibitors of ERα AF2 were identified from this study out of which, the inhibitor VPC-16230 was identified as the lead ERα AF2 inhibitor demonstrating a substantial down regulation of ERα transcriptional activity.
PubMed
Measuring Protein-Protein and Protein-Nucleic Acid Interactions by Bio-Layer Interferometry
Sultana A, Lee J, Curr Protoc Protein Sci, 79:19.25.1-19.25.26, 2015
This is a detailed write-up explaining the stepwise procedure of BLI-based advanced kinetic analyses of DNA-protein and protein-protein interactions using Pall ForteBio BLItz and the Octet systems. The preparation of the biotinylated ligands, choices for controls, assay optimization approaches, strategies applicable to regeneration of Streptavidin-based biosensors, and assay troubleshooting approaches are described. Authors recommend BLI as a versatile platform providing accurate measurements of binding affinities (KD), rates of association, and rates of dissociation (kon and koff) of protein-protein and protein-nucleic acid interactions in minutes by utilizing relatively small quantities of sample.
PubMed
Patient-Specific Neutralizing Antibody Responses to Herpes Simplex Virus are Attributed to Epitopes on Either gD, gB, or Both and Can Be Type-Specific
Cairns T, et al., J Virol, pii: JVI.01213-15, 2015
Described herein is a detailed study involving human sera obtained from HSV (Herpes simplex virus) infected patients and tests for the ability to bind to glycoproteins and compete with anti-gD and anti-gB neutralizing mAbs. Some of the examined infected individuals had no recurrent disease. A Pall ForteBio Octet RED96 instrument equipped with biotinylated glycoproteins captured onto Streptavidin biosensors was used to investigate the serum samples. Authors describe several advantages of using the Octet system as compared to the BIAcore system that was used in their previous studies. Authors recognize Octet system as a powerful method to carry out their assays. Overall results demonstrate the significance of gD and gB serotypes as immunogens, bringing new insights for future HSV vaccine development.
PubMed